Probing intra-molecular mechanics of single circularly permuted green fluorescent protein with atomic force microscopy

Tong Wang, Ken Nakajima, Atsushi Miyawaki, Masahiko Hara

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)

    Abstract

    We investigated the mechanical unfolding of single circularly permuted green fluorescent protein (cpGFP) with atomic force microscopy (AFM). The molecule was stretched from its N- and C-termini by an external force causing an elongation of the polypeptide chain up to its full length. The features of the force-extension (F-E) curves were found to depend on the stretching speed. At fast speeds, we detected one peak in the F-E curves before final rupture of the extended molecule, which we interpreted as the unfolding of two terminal halves within cpGFP. We observed several more force peaks in a sawtooth pattern at much slower speeds, and explained the appearance of such force peaks as cooperative unfolding of the hidden sub-structures inside each terminal half.

    Original languageEnglish
    Pages (from-to)90-95
    Number of pages6
    JournalUltramicroscopy
    Volume105
    Issue number1-4
    DOIs
    Publication statusPublished - 2005 Nov 1

    Keywords

    • Atomic force microscopy
    • Circular permutation
    • Green fluorescent protein
    • Mechanical unfolding
    • β-barrel

    ASJC Scopus subject areas

    • Electronic, Optical and Magnetic Materials
    • Atomic and Molecular Physics, and Optics
    • Instrumentation

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